ID A0R1X2_MYCS2 Unreviewed; 323 AA.
AC A0R1X2;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Cysteine synthase B {ECO:0000313|EMBL:ABK70074.1};
DE EC=2.5.1.47 {ECO:0000313|EMBL:ABK70074.1};
GN Name=cysM {ECO:0000313|EMBL:ABK70074.1};
GN OrderedLocusNames=MSMEG_4905 {ECO:0000313|EMBL:ABK70074.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK70074.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK70074.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR605856-50};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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DR EMBL; CP000480; ABK70074.1; -; Genomic_DNA.
DR RefSeq; WP_003896302.1; NZ_SIJM01000024.1.
DR RefSeq; YP_889160.1; NC_008596.1.
DR AlphaFoldDB; A0R1X2; -.
DR STRING; 246196.MSMEG_4905; -.
DR PaxDb; 246196-MSMEI_4778; -.
DR GeneID; 66736209; -.
DR KEGG; msm:MSMEG_4905; -.
DR PATRIC; fig|246196.19.peg.4786; -.
DR eggNOG; COG0031; Bacteria.
DR OrthoDB; 9805733at2; -.
DR Proteomes; UP000000757; Chromosome.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR005856; Cys_synth.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01136; cysKM; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF255; O-PHOSPHOSERINE SULFHYDRYLASE; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR605856-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABK70074.1}.
FT DOMAIN 8..294
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 81
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 184..188
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 323 AA; 34769 MW; 27EC06F13CFF861D CRC64;
MTRYDSLLQA LGNTPLVGLQ NLSPRWDDED GKPHVRLWAK LEDRNPTGSI KDRPALRMIE
QAERDGLLQP GATILEPTSG NTGISLAMAA LLKGYNMICV MPENTSIERR QILELYGARI
IFSPAEGGSN TAVATAKELA AQNPSWVMLY QYGNPANSDA HYFGTGPELL ADLPEITHFV
AGLGTTGTLM GTGRFLREHV PGVQIVAAEP RYGEGVYALR NIDEGFIPEL YDADVLTTRF
SVGSFDAVRR TRELVTREGI FAGISTGAVL HAALGMAAKA VKAGERADIA FVVADAGWKY
LSTGAYAGSL DDAEDALEGQ LWA
//
